Research graph
References from Discovery, Design, and Evaluation of Nanomolar to Picomolar Inhibitors of Human Pancreatic α-Amylase for Control of Postprandial Blood Glucose Levels. Local targets link to admitted publications; unresolved targets remain external evidence.
The amylase inhibitor montbretin A reveals a new glycosidase inhibition motif
10.1038/nchembio.1865 · 2015 · External reference
Potent human alpha-amylase inhibition by the beta-defensin-like protein helianthamide
10.1021/acscentsci.5b00399 · 2016 · External reference
Synthesis of montbretin A analogues yields potent competitive inhibitors of human pancreatic α-amylase
10.1039/c9sc02610j · 2019 · External reference
Rapid discovery of potent and selective glycosidase-inhibiting de novo peptides
10.1016/j.chembiol.2017.02.001 · 2017 · External reference
Milestones in the history of diabetes mellitus: The main contributors
10.4239/wjd.v7.i1.1 · 2016 · External reference
Worldwide trends in diabetes prevalence and treatment from 1990 to 2022: a pooled analysis of 1108 population-representative studies with 141 million participants
10.1016/s0140-6736(24)02317-1 · 2024 · External reference
Dual α-amylase and α-glucosidase inhibitors: recent progress from natural and synthetic resources
10.1016/j.bioorg.2025.108762 · 2025 · External reference
The carbohydrate-active enzyme database: functions and literature
10.1093/nar/gkab1045 · 2022 · External reference
Isolation, crystallization and preliminary diffraction analyses of human pancreatic alpha-amylase
10.1006/jmbi.1993.1221 · 1993 · External reference
Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris
10.1110/ps.8.3.635 · 1999 · External reference
Mechanism-based inhibition of yeast alpha-glucosidase and human pancreatic alpha-amylase by a new class of inhibitors. 2-Deoxy-2,2-difluoro-alpha-glycosides
10.1074/jbc.270.45.26778 · 1995 · External reference
Subsite mapping of the human pancreatic α-amylase active site through structural, kinetic, and mutagenesis techniques
10.1021/bi9921182 · 2000 · External reference
The structure of human pancreatic alpha-amylase at 1.8 angstrom resolution and comparisons with related enzymes
10.1002/pro.5560040908 · 1995 · External reference
Folding then binding vs folding through binding in macrocyclic peptide inhibitors of human pancreatic α-amylase
10.1021/acschembio.9b00290 · 2019 · External reference
Mechanistic analyses of catalysis in human pancreatic α-amylase: Detailed kinetic and structural studies of mutants of three conserved carboxylic acids
10.1021/bi011821z · 2002 · External reference
Glucosyl epi-cyclophellitol allows mechanism-based inactivation and structural analysis of human pancreatic α-amylase
10.1002/1873-3468.12143 · 2016 · External reference
Directed “in situ” inhibitor elongation as a strategy To structurally characterize the covalent glycosyl-enzyme intermediate of human pancreatic α-amylase
10.1021/bi901400p · 2009 · External reference
Proteinaceous α-amylase inhibitors
10.1016/j.bbapap.2003.07.004 · 2004 · External reference
The search for novel human pancreatic α-amylase inhibitors: High-throughput screening of terrestrial and marine natural product extracts
10.1002/cbic.200700470 · 2008 · External reference
Psychosocial stress-induced activation of salivary alpha-amylase: An indicator of sympathetic activity?
10.1196/annals.1314.033 · 2004 · External reference
A phenol sandwich fights diabetes
10.1038/nchembio.1888 · 2015 · External reference
Glucose lowering effect of montbretin A in zucker diabetic fatty rats
10.1007/s11010-015-2599-4 · 2016 · External reference
Discovery of UDP-glycosyltransferases and BAHD-acyltransferases involved in the biosynthesis of the antidiabetic plant metabolite montbretin A
10.1105/tpc.18.00406 · 2018 · External reference
Complete biosynthesis of the anti-diabetic plant metabolite montbretin A
10.1104/pp.20.00522 · 2020 · External reference
Improved production of the anti-diabetic metabolite montbretin A in Nicotiana benthamiana: discovery, characterization, and use of Crocosmia shikimate shunt genes
10.1111/tpj.16528 · 2024 · External reference
Branched montbretin A mimics allow derivatisation and potent amylase inhibition
10.1039/d3ob01051a · 2023 · External reference
Human β-defensins: The multi-functional natural peptide
10.1016/j.bcp.2024.116451 · 2024 · External reference
Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
10.1016/0005-2744(69)90420-3 · 1969 · External reference
Bioprospecting of sea anemones (Cnidaria, Anthozoa, Actiniaria) for β-defensin-like α-amylase inhibitors
10.3390/biomedicines11102682 · 2023 · External reference
Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 A resolution
10.1002/pro.5560061102 · 1997 · External reference
Structural dissection of helianthamide reveals the basis of its potent inhibition of human pancreatic α-amylase
10.1021/acs.biochem.8b00825 · 2018 · External reference
The RaPID platform for the discovery of pseudo-natural macrocyclic peptides
10.1021/acs.accounts.1c00391 · 2021 · External reference
Tendamistat (HOE 467), a tight-binding alpha-amylase inhibitor from Streptomyces tendae 4158. Isolation, biochemical properties
10.1111/j.1432-1033.1984.tb08221.x · 1984 · External reference
Sugar-derived amidines and congeners: structures, glycosidase inhibition and applications
10.2174/0929867329666211222164545 · 2022 · External reference
Enzymatic transition states and drug design
10.1021/acs.chemrev.8b00369 · 2018 · External reference
Flavonoids as dual-target inhibitors against alpha-glucosidase and alpha-amylase: a systematic review of in vitro studies
10.1007/s13659-023-00424-w · 2024 · External reference
Magnificamide is a new effective mammalian α-amylase inhibitor
10.1134/s1607672919060097 · 2019 · External reference
Glucosyl epi-cyclophellitol allows mechanism-based inactivation and structural analysis of human pancreatic α-amylase
10.1002/1873-3468.12143 · ExternalCitation · doi-reference
The search for novel human pancreatic α-amylase inhibitors: High-throughput screening of terrestrial and marine natural product extracts
10.1002/cbic.200700470 · ExternalCitation · doi-reference
The structure of human pancreatic alpha-amylase at 1.8 angstrom resolution and comparisons with related enzymes
10.1002/pro.5560040908 · ExternalCitation · doi-reference
Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 A resolution
10.1002/pro.5560061102 · ExternalCitation · doi-reference
Isolation, crystallization and preliminary diffraction analyses of human pancreatic alpha-amylase
10.1006/jmbi.1993.1221 · ExternalCitation · doi-reference
Glucose lowering effect of montbretin A in zucker diabetic fatty rats
10.1007/s11010-015-2599-4 · ExternalCitation · doi-reference
Flavonoids as dual-target inhibitors against alpha-glucosidase and alpha-amylase: a systematic review of in vitro studies
10.1007/s13659-023-00424-w · ExternalCitation · doi-reference
Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
10.1016/0005-2744(69)90420-3 · ExternalCitation · doi-reference
Proteinaceous α-amylase inhibitors
10.1016/j.bbapap.2003.07.004 · ExternalCitation · doi-reference
Human β-defensins: The multi-functional natural peptide
10.1016/j.bcp.2024.116451 · ExternalCitation · doi-reference
Dual α-amylase and α-glucosidase inhibitors: recent progress from natural and synthetic resources
10.1016/j.bioorg.2025.108762 · ExternalCitation · doi-reference
Rapid discovery of potent and selective glycosidase-inhibiting de novo peptides
10.1016/j.chembiol.2017.02.001 · ExternalCitation · doi-reference
Worldwide trends in diabetes prevalence and treatment from 1990 to 2022: a pooled analysis of 1108 population-representative studies with 141 million participants
10.1016/s0140-6736(24)02317-1 · ExternalCitation · doi-reference
The RaPID platform for the discovery of pseudo-natural macrocyclic peptides
10.1021/acs.accounts.1c00391 · ExternalCitation · doi-reference
Structural dissection of helianthamide reveals the basis of its potent inhibition of human pancreatic α-amylase
10.1021/acs.biochem.8b00825 · ExternalCitation · doi-reference
Enzymatic transition states and drug design
10.1021/acs.chemrev.8b00369 · ExternalCitation · doi-reference
Potent human alpha-amylase inhibition by the beta-defensin-like protein helianthamide
10.1021/acscentsci.5b00399 · ExternalCitation · doi-reference
Folding then binding vs folding through binding in macrocyclic peptide inhibitors of human pancreatic α-amylase
10.1021/acschembio.9b00290 · ExternalCitation · doi-reference
Mechanistic analyses of catalysis in human pancreatic α-amylase: Detailed kinetic and structural studies of mutants of three conserved carboxylic acids
10.1021/bi011821z · ExternalCitation · doi-reference
Directed “in situ” inhibitor elongation as a strategy To structurally characterize the covalent glycosyl-enzyme intermediate of human pancreatic α-amylase
10.1021/bi901400p · ExternalCitation · doi-reference
Subsite mapping of the human pancreatic α-amylase active site through structural, kinetic, and mutagenesis techniques
10.1021/bi9921182 · ExternalCitation · doi-reference
The amylase inhibitor montbretin A reveals a new glycosidase inhibition motif
10.1038/nchembio.1865 · ExternalCitation · doi-reference
A phenol sandwich fights diabetes
10.1038/nchembio.1888 · ExternalCitation · doi-reference
Synthesis of montbretin A analogues yields potent competitive inhibitors of human pancreatic α-amylase
10.1039/c9sc02610j · ExternalCitation · doi-reference
Branched montbretin A mimics allow derivatisation and potent amylase inhibition
10.1039/d3ob01051a · ExternalCitation · doi-reference
Mechanism-based inhibition of yeast alpha-glucosidase and human pancreatic alpha-amylase by a new class of inhibitors. 2-Deoxy-2,2-difluoro-alpha-glycosides
10.1074/jbc.270.45.26778 · ExternalCitation · doi-reference
The carbohydrate-active enzyme database: functions and literature
10.1093/nar/gkab1045 · ExternalCitation · doi-reference
Complete biosynthesis of the anti-diabetic plant metabolite montbretin A
10.1104/pp.20.00522 · ExternalCitation · doi-reference
Discovery of UDP-glycosyltransferases and BAHD-acyltransferases involved in the biosynthesis of the antidiabetic plant metabolite montbretin A
10.1105/tpc.18.00406 · ExternalCitation · doi-reference
Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris
10.1110/ps.8.3.635 · ExternalCitation · doi-reference
Tendamistat (HOE 467), a tight-binding alpha-amylase inhibitor from Streptomyces tendae 4158. Isolation, biochemical properties
10.1111/j.1432-1033.1984.tb08221.x · ExternalCitation · doi-reference
Improved production of the anti-diabetic metabolite montbretin A in Nicotiana benthamiana: discovery, characterization, and use of Crocosmia shikimate shunt genes
10.1111/tpj.16528 · ExternalCitation · doi-reference
Magnificamide is a new effective mammalian α-amylase inhibitor
10.1134/s1607672919060097 · ExternalCitation · doi-reference
Psychosocial stress-induced activation of salivary alpha-amylase: An indicator of sympathetic activity?
10.1196/annals.1314.033 · ExternalCitation · doi-reference
Sugar-derived amidines and congeners: structures, glycosidase inhibition and applications
10.2174/0929867329666211222164545 · ExternalCitation · doi-reference
Bioprospecting of sea anemones (Cnidaria, Anthozoa, Actiniaria) for β-defensin-like α-amylase inhibitors
10.3390/biomedicines11102682 · ExternalCitation · doi-reference
Milestones in the history of diabetes mellitus: The main contributors
10.4239/wjd.v7.i1.1 · ExternalCitation · doi-reference
